A variety of classical and modern techniques will be used to continue studies of bonding forces in proteins and model amides. Resonance Raman spectra of protein complexes with small molecules will be examined to see which substituents are perturbed, by, and hence involved in, binding. Volume changes will be measured for the transfer of an amide group from amide-type surroundings to water to provide a basis for understanding molecular contributions to volume changes accompanying conformational unfolding of proteins. Fluorine-19 labeled substances will also provide nuclear magnetic resonance probes of conformational changes and interactions. Studies of hydrogen-deuterium exchange rates in a polymeric amide, as affected by intrinsic and extrinsic factors, should further elucidate the features that affect this very simple chemical reaction when it takes place within a protein environment. Bibliographic references: A Two-Dimensional Representation of Protein Structures. Arch. Biochem. Biophys., 167, 615-626 (1975). J.B.R. Dunn and I.M. Klotz Quaternary Structure of Proteins. In The Proteins, Third Ed., Vol. I, pp. 293-411. Edited by H. Neutrath and R.H. Hill, Academic Press, N.Y. 1975. I.M. Klotz, D.W. Darnall, and N.R. Langerman.